Prion protein

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The prion protein (PrP) is a cell surface glycoprotein. The cellular isoform (PrP<sup>C</sup>) has two dominas: an dN-terminal region that is natively unstructured, and a C-terminal region from residues ~120-230, which is predominantly α-helical. PrP<sup>C</sup> can undergo a structural conversion to a β-sheet rich conformation, termed PrP<sup>Sc</sup>. Prion diseases such as Creutzfeldt Jakob disease (CJD) in people, and bovine spongiform encephalopathy (BSE) commonly known as "mad cow" disease, are characterterized by aggregates of PrP<sup>Sc</sup>, which arise from autocatalytic refolding of PrP<sup>C</sup> in a template-dependent manner.
The prion protein (PrP) is a cell surface glycoprotein. The cellular isoform (PrP<sup>C</sup>) has two dominas: an dN-terminal region that is natively unstructured, and a C-terminal region from residues ~120-230, which is predominantly α-helical. PrP<sup>C</sup> can undergo a structural conversion to a β-sheet rich conformation, termed PrP<sup>Sc</sup>. Prion diseases such as Creutzfeldt Jakob disease (CJD) in people, and bovine spongiform encephalopathy (BSE) commonly known as "mad cow" disease, are characterterized by aggregates of PrP<sup>Sc</sup>, which arise from autocatalytic refolding of PrP<sup>C</sup> in a template-dependent manner.
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Structure from a
 
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's normal cellular function is debated, and "knockout" mice lacking PrP are phenotypically normal.
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==Structure of PrP<sup>C</sup>==
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has a predominantly α-helical structure and is localized to the outer leaflet of the cell membrane by a glycolipid anchor. In prion diseases PrPC undergoes a major structural transformation converting . This process is autocatalytic with PrPSc driving the refolding of PrPC in a template-dependent manner, leading to accumulation of PrPSc and ultimately neuronal cell death.
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==Structure of PrPC==
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{{STRUCTURE_1hjm | PDB=1hjm | SCENE= }}
{{STRUCTURE_1hjm | PDB=1hjm | SCENE= }}
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The structure is highly conserved amongst mammals...
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The X-ray structure of sheep PrP was dimeric...
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==Models of PrP<sup>Sc</sup> structure==
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There are a number of technical obstacles in determining the molecular structure of PrP(sup)Sc</sup>
==Selected PrP structures==
==Selected PrP structures==
=Human PrP=
=Human PrP=
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* 1QLX HuPrP 23-230 Average 125-228
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* [[1QLX]] HuPrP 23-230 Average 125-228
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* 1QM0 HuPrP 90-230 Average 125-228
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* [[1QM0]] HuPrP 90-230 Average 125-228
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* 1QM2 HuPrP 121-230 Average 125-228
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* [[1QM2]] HuPrP 121-230 Average 125-228
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* 1I4M HuPrP 119-226 (X-ray) 119-226
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* [[1I4M]] HuPrP 119-226 (X-ray) 119-226
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* 1E1J HuPrP,M166V 125-228 Average 125-228
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* [[1E1J]] HuPrP,M166V 125-228 Average 125-228
* 1E1S HuPrP,S170N 125-228 Average 125-228
* 1E1S HuPrP,S170N 125-228 Average 125-228
* 1E1W HuPrP,R220K 125-228 Average 125-228
* 1E1W HuPrP,R220K 125-228 Average 125-228
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1UW3 Sheep PrP
1UW3 Sheep PrP
* XXXX Frog PrP
* XXXX Frog PrP
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* Chicken PrP
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* XXXX Chicken PrP
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* Turtle PrP
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* XXXX Turtle PrP
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==References==

Revision as of 12:50, 9 December 2008

The prion protein (PrP) is a cell surface glycoprotein. The cellular isoform (PrPC) has two dominas: an dN-terminal region that is natively unstructured, and a C-terminal region from residues ~120-230, which is predominantly α-helical. PrPC can undergo a structural conversion to a β-sheet rich conformation, termed PrPSc. Prion diseases such as Creutzfeldt Jakob disease (CJD) in people, and bovine spongiform encephalopathy (BSE) commonly known as "mad cow" disease, are characterterized by aggregates of PrPSc, which arise from autocatalytic refolding of PrPC in a template-dependent manner.

Contents

Structure of PrPC

PDB ID 1hjm

Drag the structure with the mouse to rotate
1hjm, 1 NMR models ()
Related: 1e1g, 1e1j, 1e1p, 1e1s, 1e1u, 1e1w, 1hjn
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



The structure is highly conserved amongst mammals...

The X-ray structure of sheep PrP was dimeric...

Models of PrPSc structure

There are a number of technical obstacles in determining the molecular structure of PrP(sup)Sc</sup>

Selected PrP structures

Human PrP

  • 1QLX HuPrP 23-230 Average 125-228
  • 1QM0 HuPrP 90-230 Average 125-228
  • 1QM2 HuPrP 121-230 Average 125-228
  • 1I4M HuPrP 119-226 (X-ray) 119-226
  • 1E1J HuPrP,M166V 125-228 Average 125-228
  • 1E1S HuPrP,S170N 125-228 Average 125-228
  • 1E1W HuPrP,R220K 125-228 Average 125-228
  • 1FKC HuPrP,E200K 90-231 Average 125-231
  • 1H0L HuPrP,M166C,E221C 121-230 20 structures 119-230

Other PrPs

Rodent PrP

  • XXXX Mouse PrP determined by NMR
  • 1B10 Syrian hamster PrP 90-231 NMR ensemble of 25 structures

1DWY Cow PrP 121-230 Average 124-227 1UW3 Sheep PrP

  • XXXX Frog PrP
  • XXXX Chicken PrP
  • XXXX Turtle PrP

References

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